Self-association of Band 3, the human erythrocyte anion exchanger, in detergent solution
نویسندگان
چکیده
منابع مشابه
Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3.
The electroneutral exchange of chloride and bicarbonate across the human erythrocyte membrane is facilitated by Band 3, a 911 amino acid glycoprotein consisting of a 43 kDa N-terminal cytosolic domain that binds the cytoskeleton, haemoglobin and glycolytic enzymes and a 52 kDa C-terminal membrane domain that mediates anion transport. Electron microscopy and three-dimensional image reconstructio...
متن کاملImportance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain.
Three-dimensional crystals were obtained for the membrane domain of the human erythrocyte anion exchanger (AE1, Band 3). Protein homogeneity and stability and the delicate balance between the detergent used and the amount of phospholipids copurifying are critical to the formation of three-dimensional crystals of the AE1 membrane domain. While deglycosylation improved the protein homogeneity, it...
متن کاملTransmembrane folding of the human erythrocyte anion exchanger (AE1, Band 3) determined by scanning and insertional N-glycosylation mutagenesis.
The human erythrocyte anion exchanger (AE1, Band 3) contains up to 14 transmembrane segments, with a single site of N-glycosylation at Asn642 in extracellular (EC) loop 4. Scanning and insertional N-glycosylation mutagenesis were used to determine the folding pattern of AE1 in the membrane. Full-length AE1, when expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells, retained ...
متن کاملThe structure of the human red blood cell anion exchanger (EPB3, AE1, band 3) gene.
The structure and sequence of the human red blood cell anion exchanger (EPB3, AE1, band 3) gene was determined by analysis of genomic and cDNA clones. The gene extends over 18 kb and consists of 20 exons. The cDNA sequence comprises 4,906 nucleotides [excluding the poly(A) tail]. There is extensive similarity between the human and mouse AE1 gene, although the latter covers 17 kb. The additional...
متن کاملThe human erythrocyte anion transport protein, band 3. Characterization of exofacial alkaline titratable groups involved in anion binding/translocation
Chloride self-exchange across the human erythrocyte membrane at alkaline extracellular pH (pHO) and constant neutral intracellular pH (pH(i)) can be described by an exofacial deprotonatable reciprocating anion binding site model. The conversion of the transport system from the neutral to the alkaline state is related to deprotonation of a positively charged ionic strength- and substrate-sensiti...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 1997
ISSN: 0005-2736
DOI: 10.1016/s0005-2736(97)00033-3